Transfected Stable Cell Lines
Reliable | High-Performance | Wide Rage
Precision reporter, kinase, immune receptor, biosimilar, Cas9, and knockout stable cell lines for diverse applications.
| Cat.No. | Product Name | Price |
|---|---|---|
| CSC-DC011285 | Panoply™ Human PAPD7 Knockdown Stable Cell Line | Inquiry |
| CSC-SC011285 | Panoply™ Human PAPD7 Over-expressing Stable Cell Line | Inquiry |
| Cat.No. | Product Name | Price |
|---|---|---|
| AD11793Z | Human PAPD7 adenoviral particles | Inquiry |
| LV20950L | human PAPD7 (NM_001171805) lentivirus particles | Inquiry |
| LV20951L | human PAPD7 (NM_006999) lentivirus particles | Inquiry |
| LV20952L | human PAPD7 (NM_001171806) lentivirus particles | Inquiry |
| Cat.No. | Product Name | Price |
|---|---|---|
| SHH370472 | shRNA set against Human PAPD7 (NM_006999.4) | Inquiry |
| SHH370476 | shRNA set against Mouse PAPD7 (NM_198600.2) | Inquiry |
| SHW001103 | shRNA set against Chicken PAPD7 (NM_001012950) | Inquiry |
| Cat.No. | Product Name | Price |
|---|---|---|
| CDCS419197 | Human PAPD7 ORF Clone (BC117137) | Inquiry |
| CDFH013677 | Human PAPD7 cDNA Clone(NM_001171805.1) | Inquiry |
| CDFH013678 | Human PAPD7 cDNA Clone(NM_001171806.1) | Inquiry |
| CDFR006857 | Rat Papd7 cDNA Clone(NM_001107333.1) | Inquiry |
| MiUTR4H-TG06411 | PAPD7 miRNA 3'UTR clone | Inquiry |
| CDCB162578 | Chicken PAPD7 ORF Clone (NM_001012950) | Inquiry |
| CDCB187815 | Rabbit PAPD7 ORF clone (XM_002721816.2) | Inquiry |
| CDCH016895 | Human PAPD7 ORF clone(NM_006999.4) | Inquiry |
| CDCL145851 | Mouse PAPD7 ORF clone (NM_001171805.1) | Inquiry |
| CDCL145853 | Human PAPD7 ORF clone (NM_001171806.1) | Inquiry |
| CDCR241964 | Mouse Papd7 ORF Clone(NM_001169131.1) | Inquiry |
| CDCR276475 | Mouse Papd7 ORF Clone(NM_198600.2) | Inquiry |
| CDCR374046 | Rat Papd7 ORF Clone(NM_001107333.1) | Inquiry |
| CDCS419198 | Human PAPD7 ORF Clone (BC084567) | Inquiry |
Seven proteins of the non-canonical poly(A) polymerases (ncPAPs) or the Cid1-like family contained in the Mammalian cells, as well as canonical poly(A) polymerases, were classified into the member of the polymerase β-like nucleotidyl transferase superfamily, which has homology in sequence and structure with the catalytic domain of DNA Pol β. A PAPD7-specific antibody was generated and it was found to be a protein migrated at 94 kDa on SDS-PAGE, whose isoform has N-terminal extension encoded by highly GC-rich sequence (>76%), the difference in intranuclear distributions of 94kDa PAPD7 from PAPD5 was revealed by fluorescent microscopy analysis: PAPD5 is widely distributed in the nucleoli and PAPD7 is excluded from it to accumulate into a minor pool in the cytoplasm. In the tethering assays for assay of the nucleotidyl transferase activities of those proteins, the 94kDa PAPD7 exhibited a robust nucleotidyl transferase activity than 62 kDa isoform when tethered to mRNA 3'UTR despite of both of which contain nucleotidyl transferase domain. Conserved residues of PAPD5 and PAPD7 N-terminal sequence were found to be in juxtaposition with nucleotidyl transferase domain, so the N-terminal region was narrowed to be an indispensable part for the nucleotidyl transferase activity and nuclear localization of PAPD7.
Stabilization of hepatitis B virus (HBV) RNA can be got by interactions between the noncanonical poly(A) polymerases PAPD7 and the viral posttranscriptional regulatory element (PRE). It may represent a new antiviral target for control of HBV RNA metabolism, hepatitis B surface antigen (HBsAg) production, and viral replication. Antiviral therapy was developed by targeting these proteins. A potent chemical probe along with genetic analyses was utilized to dissect the individual roles of PAPD7 in HBV RNA stability. The chemical probe can inhibit PAPD7 enzymatic activities and reduces HBsAg both in vitro and in vivo. The essential role of stem-loop alpha sequence within PRE in HBV poly(A) tail integrity maintenance and determining sensitivity toward the inhibitory of this chemical probe has been demonstrated in genetic studies. Single PAPD7 KO did not cause any measurable changes within the HBV poly(A) tails, but both PAPD5 and PAPD7 KO in cells can induce reduced HBsAg production and resistance to this chemical probe.
Figure 1. A proposed model illustrating the interplay between HBV RNA cis-elements and the host factors PAPD5 and PAPD7 in maintaining HBV integrity and stability. (Fei Liu, et al. 2021)
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